720 research outputs found
Letter from Robert E. Prior to James B. Finley
Prior writes asking Finley to help bring about the pardon of his brother James, who is in prison and very ill. Governor Bebb is aware of the situation, but Finley will need to advocate for James\u27 release. Abstract Number - 1102https://digitalcommons.owu.edu/finley-letters/2086/thumbnail.jp
Letter from Robert E. Prior to James B. Finley
Prior writes concerning his incarcerated brother, James Prior, who is ill. In order to request a pardon for James from Governor Bebb, Prior needs two letters -- one from Finley attesting to the reformation of James\u27 character, and one from the attending physician at the prison, confirming that confinement is dangerous for James\u27 health. Abstract Number - 1121https://digitalcommons.owu.edu/finley-letters/2105/thumbnail.jp
Observing Molecular Spinning via the Rotational Doppler Effect
When circularly polarized light is scattered from a rotating target, a
rotational Doppler shift (RDS) emerges from an exchange of angular momentum
between the spinning object and the electromagnetic field. Here, we used
coherently spinning molecules to generate a shift of the frequency of a
circularly polarized probe propagating through a gaseous sample. We used a
linearly polarized laser pulse to align the molecules, followed by a second
delayed pulse polarized at 45{\deg} to achieve unidirectional molecular
rotation. The measured RDS is orders of magnitude greater than previously
observed by other methods. This experiment provides explicit evidence of
unidirectional molecular rotation and paves the way for a new class of
measurements in which the rotational direction of molecular reagents may be
monitored or actively controlled.Comment: Submitted also to Nature Photonics, current status: "under
consideration
Brief Note Surface Charge Determination of Proteus Mirabilis Exposed to Carbenicillin
Author Institution: Division of Infectious Diseases, Department of Medicine, The Ohio State University College of Medicin
Direct visualization of Ras proteins in spatially distinct cell surface microdomains
Localization of signaling complexes to specific microdomains coordinates signal transduction at the plasma membrane. Using immunogold electron microscopy of plasma membrane sheets coupled with spatial point pattern analysis, we have visualized morphologically featureless microdomains, including lipid rafts, in situ and at high resolution. We find that an inner-plasma membrane lipid raft marker displays cholesterol-dependent clustering in microdomains with a mean diameter of 44 nm that occupy 35% of the cell surface. Cross-linking an outer-leaflet raft protein results in the redistribution of inner leaflet rafts, but they retain their modular structure. Analysis of Ras microlocalization shows that inactive H-ras is distributed between lipid rafts and a cholesterol-independent microdomain. Conversely, activated H-ras and K-ras reside predominantly in nonoverlapping, cholesterol-independent microdomains. Galectin-1 stabilizes the association of activated H-ras with these nonraft microdomains, whereas K-ras clustering is supported by farnesylation, but not geranylgeranylation. These results illustrate that the inner plasma membrane comprises a complex mosaic of discrete microdomains. Differential spatial localization within this framework can likely account for the distinct signal outputs from the highly homologous Ras proteins
Collective Plasmonic-Molecular Modes in the Strong Coupling Regime
We demonstrate strong coupling between molecular excited states and surface
plasmon modes of a slit array in a thin metal film. The coupling manifests
itself as an anti-crossing behavior of the two newly formed polaritons. As the
coupling strength grows, a new mode emerges, which is attributed to long range
molecular interactions mediated by the plasmonic field. The new, molecular-like
mode repels the polariton states, and leads to an opening of energy gaps both
below and above the asymptotic free molecule energy.Comment: 8 pages, 6 figures, submitted to PR
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